
Name the molecule acting as energy currency in organisms.
Answer
514.5k+ views
Hint: This is the principle energy-generating procedure found in all forms of life and is the fuel for the operation of almost all metabolic pathways of the cell. In this structure, the presence of two high-energy phosphate bonds, called phosphoanhydride bonds, are liable for high energy content.
Complete answer:
-As “molecular currency” for intracellular energy transfer, ATP (ATP) functions as a chemical fuel by powering many organic processes of life.
-In an ATP molecule structure, the presence of two high-energy phosphate bonds, called phosphoanhydride bonds, are responsible for high energy content.
-Hydrolysis of the third phosphate group of adenosine diphosphate (ADP) and inorganic phosphate (Pi), along with the considerable release of energy.
-ADP can absorb energy and regain the group to regenerate an ATP molecule to take care of constant ATP concentration.
-The aggregate amount of ATP in the human body present is about 0.1 Mole.
-ATP cannot be stored and thus its synthesis is closely linked to its consumption.
-ATP is production is under aerobic conditions through glycolysis, citric acid cycle/oxidative phosphorylation, and beta-oxidation and under anaerobic conditions through fermentation, photophosphorylation, and replenishment reactions catalyzed by nucleoside diphosphate kinase.
Additional Information:
ATP synthase
-ATP is synthesized from its precursor which is adenosine diphosphate ADP, by ATP synthases. These enzymes are found within the cristae and therefore the inner membrane of mitochondria, the thylakoid membrane of chloroplasts, and therefore the cell wall of bacteria.
-In the case of bacteria and archaebacteria who lack mitochondria have mesosome, ATP synthase is found in their plasma membrane.
Disease-related to ATP synthase
-The first defect in ATP synthase was reported by Houstek by the result of a case study of a child with severe lactic acidosis, cardiomyopathy, and hepatomegaly, who died 2 days after birth.
-The enzyme was under-expressed by 70-80% and there was no observed mutation or expression deficit in the enzyme.
-The mutations in some factors explicitly involved within the assembly of ATP synthase could have caused the defect.
-The mutations in both the nuclear and mitochondrial DNA.
-A mutation in one or many within the subunits in ATPase synthase can cause these diseases.
Note: -A drug, diarylquinoline which is also known as TMC207 developed against tuberculosis is known to block the synthesis of ATP by targeting subunit c of ATP synthase of tuberculosis bacteria.
-ATP synthase inhibitors, Bz-423 is pro-apoptotic and 1,4-benzodiazepine binds the oligomycin sensitivity conferring protein (OSCP) component resulting in the generation of superoxide and subsequent apoptosis.
Complete answer:
-As “molecular currency” for intracellular energy transfer, ATP (ATP) functions as a chemical fuel by powering many organic processes of life.
-In an ATP molecule structure, the presence of two high-energy phosphate bonds, called phosphoanhydride bonds, are responsible for high energy content.
-Hydrolysis of the third phosphate group of adenosine diphosphate (ADP) and inorganic phosphate (Pi), along with the considerable release of energy.
-ADP can absorb energy and regain the group to regenerate an ATP molecule to take care of constant ATP concentration.
-The aggregate amount of ATP in the human body present is about 0.1 Mole.
-ATP cannot be stored and thus its synthesis is closely linked to its consumption.
-ATP is production is under aerobic conditions through glycolysis, citric acid cycle/oxidative phosphorylation, and beta-oxidation and under anaerobic conditions through fermentation, photophosphorylation, and replenishment reactions catalyzed by nucleoside diphosphate kinase.
Additional Information:
ATP synthase
-ATP is synthesized from its precursor which is adenosine diphosphate ADP, by ATP synthases. These enzymes are found within the cristae and therefore the inner membrane of mitochondria, the thylakoid membrane of chloroplasts, and therefore the cell wall of bacteria.
-In the case of bacteria and archaebacteria who lack mitochondria have mesosome, ATP synthase is found in their plasma membrane.
Disease-related to ATP synthase
-The first defect in ATP synthase was reported by Houstek by the result of a case study of a child with severe lactic acidosis, cardiomyopathy, and hepatomegaly, who died 2 days after birth.
-The enzyme was under-expressed by 70-80% and there was no observed mutation or expression deficit in the enzyme.
-The mutations in some factors explicitly involved within the assembly of ATP synthase could have caused the defect.
-The mutations in both the nuclear and mitochondrial DNA.
-A mutation in one or many within the subunits in ATPase synthase can cause these diseases.
Note: -A drug, diarylquinoline which is also known as TMC207 developed against tuberculosis is known to block the synthesis of ATP by targeting subunit c of ATP synthase of tuberculosis bacteria.
-ATP synthase inhibitors, Bz-423 is pro-apoptotic and 1,4-benzodiazepine binds the oligomycin sensitivity conferring protein (OSCP) component resulting in the generation of superoxide and subsequent apoptosis.

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